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Database: UniProt
Entry: A0A377R2W1_9NEIS
LinkDB: A0A377R2W1_9NEIS
Original site: A0A377R2W1_9NEIS 
ID   A0A377R2W1_9NEIS        Unreviewed;       418 AA.
AC   A0A377R2W1;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=NADH-quinone oxidoreductase subunit D {ECO:0000256|HAMAP-Rule:MF_01358};
DE            EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01358};
DE   AltName: Full=NADH dehydrogenase I subunit D {ECO:0000256|HAMAP-Rule:MF_01358};
DE   AltName: Full=NDH-1 subunit D {ECO:0000256|HAMAP-Rule:MF_01358};
GN   Name=nuoD {ECO:0000256|HAMAP-Rule:MF_01358,
GN   ECO:0000313|EMBL:STR02554.1};
GN   ORFNames=NCTC13336_01431 {ECO:0000313|EMBL:STR02554.1};
OS   Kingella potus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Kingella.
OX   NCBI_TaxID=265175 {ECO:0000313|EMBL:STR02554.1, ECO:0000313|Proteomes:UP000254293};
RN   [1] {ECO:0000313|EMBL:STR02554.1, ECO:0000313|Proteomes:UP000254293}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC13336 {ECO:0000313|EMBL:STR02554.1,
RC   ECO:0000313|Proteomes:UP000254293};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC       (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC       electron acceptor for the enzyme in this species is believed to be
CC       ubiquinone. Couples the redox reaction to proton translocation (for
CC       every two electrons transferred, four hydrogen ions are translocated
CC       across the cytoplasmic membrane), and thus conserves the redox energy
CC       in a proton gradient. {ECO:0000256|HAMAP-Rule:MF_01358}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) +
CC         NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01358};
CC   -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits NuoB, C,
CC       D, E, F, and G constitute the peripheral sector of the complex.
CC       {ECO:0000256|HAMAP-Rule:MF_01358}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01358};
CC       Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01358};
CC       Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01358}.
CC   -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00005769, ECO:0000256|HAMAP-Rule:MF_01358,
CC       ECO:0000256|RuleBase:RU003685}.
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DR   EMBL; UGJJ01000002; STR02554.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A377R2W1; -.
DR   OrthoDB; 9801496at2; -.
DR   Proteomes; UP000254293; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.645.10; Cytochrome-c3 Hydrogenase, chain B; 1.
DR   HAMAP; MF_01358; NDH1_NuoD; 1.
DR   InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR   InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS.
DR   InterPro; IPR022885; NDH1_su_D/H.
DR   InterPro; IPR029014; NiFe-Hase_large.
DR   NCBIfam; TIGR01962; NuoD; 1.
DR   PANTHER; PTHR11993:SF10; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11993; NADH-UBIQUINONE OXIDOREDUCTASE 49 KDA SUBUNIT; 1.
DR   Pfam; PF00346; Complex1_49kDa; 1.
DR   SUPFAM; SSF56762; HydB/Nqo4-like; 1.
DR   PROSITE; PS00535; COMPLEX1_49K; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01358};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01358};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01358};
KW   Oxidoreductase {ECO:0000313|EMBL:STR02554.1};
KW   Quinone {ECO:0000256|HAMAP-Rule:MF_01358};
KW   Reference proteome {ECO:0000313|Proteomes:UP000254293};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW   Rule:MF_01358};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01358};
KW   Ubiquinone {ECO:0000256|HAMAP-Rule:MF_01358}.
FT   DOMAIN          121..418
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /evidence="ECO:0000259|Pfam:PF00346"
SQ   SEQUENCE   418 AA;  47457 MW;  48F5DF3D036CE1F4 CRC64;
     MATKLRNYTI NFGPQHPAAH GVLRMILELE GETIVRADPH IGLLHRGTEK LAETRTYLQA
     LPYMDRLDYV SMMVNEQAYC LAVERLTGTE VPIRGQYIRT MFAEVTRILN HLMGIGSHAL
     DIGAMTAILY AFRDREELMD LYEAVSGARM HAAYFRPGGV YRDLPDFMPK YESSKFRNAK
     VLKELNEARE GTMLDFIDAF CQRFPGRIDT LETLLTDNRI WKQRTVGIGV VTPERALQKG
     FTGVMLRGSG IEWDIRKKAP YDAYANVDFD IPVGVNGDCY DRYLCRINEM RQSVRIIQQC
     SDWLKHNPGP VITGDHKIAP PKRTDMKLGM EDLIHHFKLF TEGMHVPEGE VYAAVEHPKG
     EFGIYMISDG ANKPYRLKIR APGFAHLQGM DEMARGHMLA DVVAIIGTQD IVFGEVDR
//
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